NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Salivary gland;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).

[2]

FUNCTION IN MALIGNANT CELL GROWTH.
DOI=10.1038/sj.emboj.7600345; PubMed=15282551 [NCBI, ExPASy, EBI, Israel, Japan]
Leenders F., Moepert K., Schmiedeknecht A., Santel A., Czauderna F., Aleku M., Penschuck S., Dames S., Sternberger M., Roehl T., Wellmann A., Arnold W., Giese K., Kaufmann J., Klippel A.;
"PKN3 is required for malignant prostate cell growth downstream of activated PI 3-kinase.";
EMBO J. 23:3303-3313(2004).

Comments

FUNCTION: Contributes to invasiveness in malignant prostate cancer.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
ENZYME REGULATION: Two specific sites, Thr-707 (activation loop of the kinase domain) and Thr-849 (turn motif), need to be phosphorylated for its full activation (By similarity).
SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, perinuclear region (By similarity). Note=Nuclear and perinuclear Golgi region (By similarity).
DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
PTM: Autophosphorylated (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.
SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
SIMILARITY: Contains 1 protein kinase domain.
SIMILARITY: Contains 3 REM (Hr1) repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC034126; AAH34126.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_722500.1; -.

UniGene

Mm.233843

3D structure databases

HSSP

P31751; 1GZK. [HSSP ENTRY / PDB]

ModBase

Q8K045.

PTM databases

PhosphoSite

Q8K045; -.

Organism-specific databases

MGI

MGI:2388285; Pkn3.

Gene expression databases

CleanEx

MM_PKN3; -.

GermOnline

ENSMUSG00000026785; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004697;	Molecular function: protein kinase C activity (inferred from electronic annotation from EC).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0007165;	Biological process: signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000861; HR1-like_rho-bd.
IPR011072; HR1_rho-bd.
IPR000961; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.287.160; HR1_rho-bd; 3.

Pfam

PF02185; HR1; 3.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00742; Hr1; 3.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8K045.

Genome annotation databases

Ensembl

ENSMUSG00000026785; Mus musculus. [Contig view]

GeneID

263803; -.

KEGG

mmu:263803; -.

Phylogenomic databases

HOGENOM

Q8K045; -.

HOVERGEN

Q8K045; -.

Other

NextBio

392137; -.

SOURCE

Pkn3; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 878`	`878`	`Serine/threonine-protein kinase N3.`	`PRO_0000055726`
`REPEAT`	`15 87`	`73`	`REM 1.`
`REPEAT`	`98 169`	`72`	`REM 2.`
`REPEAT`	`171 249`	`79`	`REM 3.`
`DOMAIN`	`548 807`	`260`	`Protein kinase.`
`DOMAIN`	`808 878`	`71`	`AGC-kinase C-terminal.`
`NP_BIND`	`554 562`	`9`	`ATP (By similarity).`
`COMPBIAS`	`456 543`	`88`	`Pro-rich.`
`ACT_SITE`	`673 673`		`Proton acceptor (By similarity).`
`BINDING`	`577 577`		`ATP (By similarity).`
`MOD_RES`	`539 539`		`Phosphothreonine (By similarity).`
`MOD_RES`	`707 707`		`Phosphothreonine (By similarity).`
`MOD_RES`	`849 849`		`Phosphothreonine (Probable).`

Sequence information

Length: 878 AA [This is the length of the unprocessed precursor]

Molecular weight: 97881 Da [This is the MW of the unprocessed precursor]

CRC64: F4DC174A6E89047D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEHRKPGTGQ RAPKDEKEMV RRAIQKELKI KEGMENMRRV ATDRRHLGHV QQLLRASNRR 

        70         80         90        100        110        120 
LEQLHGELRE LHAQVLLPAS AEPVTSEPQP RAEQSRARLS EALHRQLQVE LKVKQGAENM 

       130        140        150        160        170        180 
IHTCASGTPK ERKLLAAAQQ MLKDSQLKVA LLRMKISSLE SSGSPEPGPD LLAEELQHRL 

       190        200        210        220        230        240 
RVEAAVAAGA KNVVKLLGGQ RMQDRKALAE AQAQLQESSQ KLDLLRLALE LLLERLPPTH 

       250        260        270        280        290        300 
SLRSRVTQEL WMAMLGNPQP LGTLVKPIAL TGTLQVRLLG CKDLLVAVPG RSPMAVLAGS 

       310        320        330        340        350        360 
PSESWLRTRS RQQRGGGELA SEVLAVLKVD NRVVGQTGWG LVAEKSWDQS FIISLDRARE 

       370        380        390        400        410        420 
LEIGVHWRDW RQLCGVAFLK LEDFLDNACH QLSLSLVPQG RLFAQVTFCE PVIERRPRLQ 

       430        440        450        460        470        480 
RQRCIFSKRR GRDFMRASQM NLSMAAWGRL VMSLLPPCSS PNTASPPKGR PSTAVCGTPS 

       490        500        510        520        530        540 
AASPSNFLPM KTLSKEDTKP PPKPPRLYLQ EPAPGTPCTK RPHMDPRPAV VPALAALSTR 

       550        560        570        580        590        600 
KPPRLQDFRC LAVLGRGHFG KVLLVQYKGT GKYYAIKALK KQEVLGRDEI DSLYCEKRIL 

       610        620        630        640        650        660 
ETVGRTGHPF LLSLLACLQT SSHACFVTEF LPGGDLMAQI HEDVFPEPQA CFYLACVVLG 

       670        680        690        700        710        720 
LQFLHEKRII YRDLKLDNLL LDAQGFLKIA DFGLCKEGIG FGDRTSTFCG TPEFLAPEVL 

       730        740        750        760        770        780 
TQEAYTRAVD WWGLGVLLYE MLVGECPFPG DTEEEVFECI VSADVPCPHF LSVQGLELIQ 

       790        800        810        820        830        840 
KLLQKSPEKR LGAGERDAEE IKVQPFFRTT NWQALLARTV QPPFVPTLCG PADLRYFEGE 

       850        860        870 
FTSLPPTLTP PVSQSSLTAR QQAAFRDFDF VSEQFLES

Q8K045 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools